The molybdopterin family of enzymes plays a vital role in many metabolic reactions involving redox reactions of sulfur and nitrogen centers in diverse substrates, including nitrogen assimilation in plants[1] and the anaerobic respiration of many bacteria[2]. In humans, deficiency in molybdopterin enzymes like sulfite oxidase causes fatal neurological damage[3]. Despite the biological importance of these enzymes, much about their structure and activity remains unknown. Their most unusual feature, a pterin-substituted dithiolene chelating the central metal ion, was conclusively determined within the past decade[4], and it is suspected that pterin redox reactions play an important role in molybdoenzyme function.

This summer in the Burgmayer lab, I will be working together with Amy Rothkopf to synthesize molybdenum pterinyl-dithiolene complexes analogous to the molybdopterin portion of the molybdenum cofactor from the metal sulfido tetrasulfide precursor Tp*MoIV(S)(S4)-and three different pivalated pterinyl alkynes, designated AEPa, IPEPP and DIFPEPP (synthesized by Candi Greeman). In addition to exploring the effects of the various substituents on the redox chemistry of the pterinyl portions of the complexes using a variety of spectroscopic techniques, I will be working towards refining the efficiencies of these reactions, increasing their yields and purities.